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UniProtKB/Swiss-Prot entry Q3JFK2

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ASPD_BURP1
Primary accession number Q3JFK2
Secondary accession numbers None
Integrated into Swiss-Prot on February 5, 2008
Sequence was last modified on November 8, 2005 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 20)
Name and origin of the protein
Protein name Probable L-aspartate dehydrogenase
Synonym EC 1.4.1.21
Gene name
Name: nadX
OrderedLocusNames: BURPS1710b_A2501
From
Burkholderia pseudomallei (strain 1710b) [TaxID: 320372] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei group.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Woods D.E., Nierman W.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
CP000125; ABA53762.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_337651.1; -.
3D structure databases
ModBase Q3JFK2.
Enzyme and pathway databases
BioCyc BPSE320372:BURPS1710B_B2937-MON; -.
Ontologies
GO
GO:0051287; Molecular function: NAD binding (inferred from electronic annotation from HAMAP).
GO:0050661; Molecular function: NADP binding (inferred from electronic annotation from HAMAP).
GO:0016639; Molecular function: oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor (inferred from electronic annotation from HAMAP).
GO:0009435; Biological process: NAD biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_01265; -; 1.
PBIL [Tree]
InterPro IPR005106; Asp/hSer_DHase_NAD-bd.
IPR002811; Asp_DHase.
IPR011182; Asp_DHase_NAD_syn.
Graphical view of domain structure.
Pfam PF01958; DUF108; 1.
PF03447; NAD_binding_3; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF005227; Asp_dh_NAD_syn; 1.
ProDom PD017325; Asp_dh; 1.
[Domain structure / List of seq. sharing at least 1 domain]
BLOCKS Q3JFK2.
Genome annotation databases
GeneID 3693319; -.
GenomeReviews CP000125_GR; BURPS1710b_A2501.
KEGG bpm:BURPS1710b_A2501; -.
TIGR BURPS1710b_A2501; -.
Phylogenomic databases
HOGENOM Q3JFK2; -.
Other
ProtoNet Q3JFK2.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; NAD; NADP; Oxidoreductase; Pyridine nucleotide biosynthesis.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   271  271     Probable L-aspartate dehydrogenase. PRO_1000067298
ACT_SITE   224   224        By similarity. 
BINDING   128   128        NAD; via amide nitrogen (By similarity). 
BINDING   194   194        NAD (By similarity). 
Sequence information
Length: 271 AA [This is the length of the unprocessed precursor] Molecular weight: 27761 Da [This is the MW of the unprocessed precursor] CRC64: 4FB855C9F3D2D311 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MRNAHAPVDV AMIGFGAIGA AVYRAVEHDA ALRVAHVIVP EHQCDAVRGA LGERVDVVSS 

        70         80         90        100        110        120 
VDALACRPQF ALECAGHGAL VDHVVPLLKA GTDCAVASIG ALSDLALLDA LSNAADAGGA 

       130        140        150        160        170        180 
TLTLLSGAIG GIDALAAARQ GGLDEVRYIG RKPPLGWLGT PAEAICDLRA MAAEQTIFEG 

       190        200        210        220        230        240 
SARDAAQLYP RNANVAATIA LAGVGLDATR VCLIADPAVT RNVHRIVARG AFGEMSIEMS 

       250        260        270 
GKPLPDNPKT SALTAFSAIR ALRNRASHCV I
Q3JFK2 in FASTA format

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